1dl6
From Proteopedia
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SOLUTION STRUCTURE OF HUMAN TFIIB N-TERMINAL DOMAIN
Overview
Transcription factor IIB (TFIIB) is an essential component in the, formation of the transcription initiation complex in eucaryal and archaeal, transcription. TFIIB interacts with a promoter complex containing the, TATA-binding protein (TBP) to facilitate interaction with RNA polymerase, II (RNA pol II) and the associated transcription factor IIF (TFIIF). TFIIB, contains a zinc-binding motif near the N-terminus that is directly, involved in the interaction with RNA pol II/TFIIF and plays a crucial role, in selecting the transcription initiation site. The solution structure of, the N-terminal residues 2-59 of human TFIIB was determined by, multidimensional NMR spectroscopy. The structure consists of a nearly, tetrahedral Zn(Cys)3(His)1 site confined by type I and "rubredoxin" turns, three antiparallel beta-strands, and disordered loops. The structure is, similar to the reported zinc-ribbon motifs in several, transcription-related proteins from archaea and eucarya, including, Pyrococcus furiosus transcription factor B (PfTFB), human and yeast, transcription factor IIS (TFIIS), and Thermococcus celer RNA polymerase II, subunit M (TcRPOM). The zinc-ribbon structure of TFIIB, in conjunction, with the biochemical analyses, suggests that residues on the beta-sheet, are involved in the interaction with RNA pol II/TFIIF, while the, zinc-binding site may increase the stability of the beta-sheet.
About this Structure
1DL6 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription., Chen HT, Legault P, Glushka J, Omichinski JG, Scott RA, Protein Sci. 2000 Sep;9(9):1743-52. PMID:11045620
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